ID A0A2J6MMB0_9BURK Unreviewed; 762 AA.
AC A0A2J6MMB0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:PLZ00732.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:PLZ00732.1};
GN ORFNames=CY652_19950 {ECO:0000313|EMBL:PLZ00732.1};
OS Burkholderia sp. WAC0059.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2066022 {ECO:0000313|EMBL:PLZ00732.1, ECO:0000313|Proteomes:UP000243676};
RN [1] {ECO:0000313|EMBL:PLZ00732.1, ECO:0000313|Proteomes:UP000243676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC0059 {ECO:0000313|EMBL:PLZ00732.1,
RC ECO:0000313|Proteomes:UP000243676};
RA Cho S.-T., Yang Y., Chen C.-L., Wang T.-F., Kuo C.-H.;
RT "Genome Sequence of Burkholderia sp. WAC0059.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLZ00732.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PNEO01000021; PLZ00732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6MMB0; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000243676; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2,
KW ECO:0000256|RuleBase:RU003427};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PLZ00732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243676}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 762 AA; 81495 MW; EE4B1947E82182FB CRC64;
MDEQLKQSAL AYHQNPRPGK ISVTPTKPLS NQLDLSLAYS PGVAAACMAI HADPLDAQKY
TSRGNLVGVV TNGTAVLGLG NIGPLAAKPV MEGKGCLFKK FAGIDVFDIE LNESDPDKLV
EAIAMLEPTL GGINLEDIKA PECFYIEKKL RERMKIPVFH DDQHGTAIIA SAAILNGLKV
VGKDLGGVKL VCSGAGAAAI ACLDLLRDLG LKKENILVAD SKGVIYEGRG QLDPTKARYA
ATTDARTLAD AVKGADVFLG CSSAGVLKPE MVKEMADRPL ILALANPEPE IRPEEAKKVR
PDAIIATGRS DYPNQVNNVL CFPFIFRGAL DVGATTITEE MKLAAVRAIA ELAQDADQGD
EVAKAYEGHS LEFGPEYLIP KPFDPRLIIK IAPAVAQAAM DSGVATRPIA DMDAYREQLG
ATVYRTGMVM RPVFAAAKAR PARIVFAEGE DERVLRAAQF VLTEKIAKPI IVGRPAVVEM
RLKKIGSKLR AGEDFEIVDP EDDPRYQKCW QAYHEIGARE GVTPEGAKAA LRKFNTLIGA
ILVHLGDADG MICGMIDSFD THLKFVRQVF GQAQQAENYA AMNLLMLPGR NLFICDTYVN
EVPSAQLLAD MTILAAREIE KFGIAPKVAL LSNSNFGSIA SVSAQRMAEA RRLLAERAPQ
LEVDGEMHGD AALSEAIRKQ AFPGTAFSGE ANLLVMPNVE AANITYNLLK MVSGEGVTVG
PFLLGTTRPV HILTPAATVR RIINMTAVAS ANAAANAAAG AR
//
